URH1_ARATH
ID URH1_ARATH Reviewed; 336 AA.
AC Q9SJM7; Q940Q6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Uridine nucleosidase 1 {ECO:0000303|PubMed:19293370};
DE EC=3.2.2.3 {ECO:0000269|PubMed:19293370};
DE AltName: Full=Adenosine nucleosidase {ECO:0000303|PubMed:19293370};
DE EC=3.2.2.7 {ECO:0000269|PubMed:19293370};
DE AltName: Full=Inosine nucleosidase {ECO:0000303|PubMed:19293370};
DE EC=3.2.2.2 {ECO:0000269|PubMed:19293370};
DE AltName: Full=Nucleoside hydrolase 1 {ECO:0000303|PubMed:21235647};
DE AltName: Full=Uridine ribohydrolase 1 {ECO:0000303|PubMed:19293370};
DE AltName: Full=Xanthosine nucleosidase {ECO:0000303|PubMed:21235647};
DE EC=3.2.2.- {ECO:0000269|PubMed:21235647, ECO:0000269|PubMed:30787180};
GN Name=URH1 {ECO:0000303|PubMed:19293370};
GN Synonyms=NSH1 {ECO:0000303|PubMed:21235647};
GN OrderedLocusNames=At2g36310 {ECO:0000312|Araport:AT2G36310};
GN ORFNames=F2H17.8 {ECO:0000312|EMBL:AAD21435.2};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19293370; DOI=10.1105/tpc.108.062612;
RA Jung B., Florchinger M., Kunz H.H., Traub M., Wartenberg R., Jeblick W.,
RA Neuhaus H.E., Mohlmann T.;
RT "Uridine-ribohydrolase is a key regulator in the uridine degradation
RT pathway of Arabidopsis.";
RL Plant Cell 21:876-891(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21599668; DOI=10.1111/j.1469-8137.2011.03711.x;
RA Riegler H., Geserick C., Zrenner R.;
RT "Arabidopsis thaliana nucleosidase mutants provide new insights into
RT nucleoside degradation.";
RL New Phytol. 191:349-359(2011).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=21235647; DOI=10.1111/j.1365-313x.2010.04455.x;
RA Jung B., Hoffmann C., Moehlmann T.;
RT "Arabidopsis nucleoside hydrolases involved in intracellular and
RT extracellular degradation of purines.";
RL Plant J. 65:703-711(2011).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, SUBUNIT, INTERACTION WITH URH2, MUTAGENESIS OF ASP-29, AND
RP ACTIVE SITE.
RC STRAIN=cv. Columbia;
RX PubMed=30787180; DOI=10.1105/tpc.18.00899;
RA Baccolini C., Witte C.-P.;
RT "AMP and GMP catabolism in Arabidopsis converge on xanthosine, which is
RT degraded by a nucleoside hydrolase heterocomplex.";
RL Plant Cell 31:734-751(2019).
CC -!- FUNCTION: Involved in purine and pyrimidine breakdown rather than in
CC pyrimidine salvage, especially in response to dark stress
CC (PubMed:19293370, PubMed:21235647, PubMed:21599668, PubMed:30787180).
CC Together with URH2, required for efficient inosine and xanthosine
CC hydrolytic activities (PubMed:21599668, PubMed:30787180). Unable to use
CC cytidine as a substrate (PubMed:19293370). Can use uridine, inosine,
CC adenosine as well as the cytokinin derivative isopentenyladenine-
CC riboside as substrates (PubMed:19293370). Hydrolyzes also xanthosine
CC with high efficiency (PubMed:21235647). {ECO:0000269|PubMed:19293370,
CC ECO:0000269|PubMed:21235647, ECO:0000269|PubMed:21599668,
CC ECO:0000269|PubMed:30787180}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + uridine = D-ribose + uracil; Xref=Rhea:RHEA:15577,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:47013; EC=3.2.2.3;
CC Evidence={ECO:0000269|PubMed:19293370};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + xanthosine = D-ribose + xanthine; Xref=Rhea:RHEA:27994,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17712, ChEBI:CHEBI:18107,
CC ChEBI:CHEBI:47013; Evidence={ECO:0000269|PubMed:21235647,
CC ECO:0000269|PubMed:30787180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + inosine = D-ribose + hypoxanthine; Xref=Rhea:RHEA:16657,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596,
CC ChEBI:CHEBI:47013; EC=3.2.2.2;
CC Evidence={ECO:0000269|PubMed:19293370};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + H2O = adenine + D-ribose; Xref=Rhea:RHEA:18669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:47013; EC=3.2.2.7;
CC Evidence={ECO:0000269|PubMed:19293370};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for uridine {ECO:0000269|PubMed:19293370};
CC KM=1.4 mM for inosine {ECO:0000269|PubMed:19293370};
CC KM=0.7 mM for adenosine {ECO:0000269|PubMed:19293370};
CC KM=0.4 mM for isopentenyladenine-riboside
CC {ECO:0000269|PubMed:19293370};
CC KM=1.69 mM for xanthosine {ECO:0000269|PubMed:21235647};
CC KM=0.44 mM for methyluridine {ECO:0000269|PubMed:21235647};
CC KM=0.52 mM for xanthosine {ECO:0000269|PubMed:30787180};
CC KM=0.73 mM for uridine {ECO:0000269|PubMed:30787180};
CC KM=0.06 mM for xanthosine (when in complex with URH2)
CC {ECO:0000269|PubMed:30787180};
CC KM=4.30 mM for uridine (when in complex with URH2)
CC {ECO:0000269|PubMed:30787180};
CC KM=0.60 mM for inosine (when in complex with URH2)
CC {ECO:0000269|PubMed:30787180};
CC Vmax=18.281 mmol/h/mg enzyme with uridine as substrate
CC {ECO:0000269|PubMed:19293370};
CC Vmax=0.869 mmol/h/mg enzyme with inosine as substrate
CC {ECO:0000269|PubMed:19293370};
CC Vmax=0.028 mmol/h/mg enzyme with adenosine as substrate
CC {ECO:0000269|PubMed:19293370};
CC Vmax=0.005 mmol/h/mg enzyme with isopentenyladenine-riboside as
CC substrate {ECO:0000269|PubMed:19293370};
CC Note=kcat is 2.65 sec(-1) with xanthosine as substrate
CC (PubMed:30787180). kcat is 33.5 sec(-1) with uridine as substrate
CC (PubMed:30787180). kcat is 23.3 sec(-1) with xanthosine as substrate
CC (when in complex with URH2) (PubMed:30787180). kcat is 55.3 sec(-1)
CC with uridine as substrate (when in complex with URH2)
CC (PubMed:30787180). kcat is 42.3 sec(-1) with inosine as substrate
CC (when in complex with URH2) (PubMed:30787180).
CC {ECO:0000269|PubMed:30787180};
CC -!- SUBUNIT: Homodimer (PubMed:30787180). Component of the NSH
CC heterocomplex made of URH1/NSH1 and URH2/NSH2 which exhibits strong
CC xanthosine nucleosidase activity (PubMed:30787180). Interacts with URH2
CC (PubMed:30787180). {ECO:0000269|PubMed:30787180}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19293370}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in leaves, flowers, stems,
CC pollen cells, root tip meristem and root vasculature.
CC {ECO:0000269|PubMed:19293370, ECO:0000269|PubMed:30787180}.
CC -!- DISRUPTION PHENOTYPE: Normal seedling germination and plant growth and
CC development in standard conditions, despite an abnormal accumulation in
CC the roots of uridine and of other pyrimidine metabolites as well as of
CC xanthosine, but no accumulation of inosine (PubMed:21599668).
CC Accelerated senescence accompanied by marked accumulation of uridine
CC and xanthosine under conditions of prolonged darkness leading to pale
CC green/yellow plants due to increased chlorophyll degradation
CC (PubMed:21235647). The roots of the double mutant urh1 urh2 accumulates
CC strong levels of xanthosine (PubMed:21599668, PubMed:30787180).
CC {ECO:0000269|PubMed:21235647, ECO:0000269|PubMed:21599668,
CC ECO:0000269|PubMed:30787180}.
CC -!- SIMILARITY: Belongs to the IUNH family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006921; AAD21435.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09231.1; -; Genomic_DNA.
DR EMBL; AY054182; AAL06843.1; -; mRNA.
DR EMBL; AY066040; AAL47407.1; -; mRNA.
DR EMBL; AY086551; AAM63615.1; -; mRNA.
DR PIR; B84779; B84779.
DR RefSeq; NP_565843.1; NM_129188.4.
DR AlphaFoldDB; Q9SJM7; -.
DR SMR; Q9SJM7; -.
DR BioGRID; 3548; 1.
DR STRING; 3702.AT2G36310.1; -.
DR PaxDb; Q9SJM7; -.
DR PRIDE; Q9SJM7; -.
DR ProteomicsDB; 228698; -.
DR EnsemblPlants; AT2G36310.1; AT2G36310.1; AT2G36310.
DR GeneID; 818204; -.
DR Gramene; AT2G36310.1; AT2G36310.1; AT2G36310.
DR KEGG; ath:AT2G36310; -.
DR Araport; AT2G36310; -.
DR TAIR; locus:2049435; AT2G36310.
DR eggNOG; KOG2938; Eukaryota.
DR HOGENOM; CLU_036838_2_1_1; -.
DR InParanoid; Q9SJM7; -.
DR OMA; HFNGGNI; -.
DR OrthoDB; 824591at2759; -.
DR PhylomeDB; Q9SJM7; -.
DR BioCyc; ARA:AT2G36310-MON; -.
DR BioCyc; MetaCyc:AT2G36310-MON; -.
DR BRENDA; 3.2.2.3; 399.
DR BRENDA; 3.2.2.8; 399.
DR PRO; PR:Q9SJM7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJM7; baseline and differential.
DR Genevisible; Q9SJM7; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0047622; F:adenosine nucleosidase activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0047724; F:inosine nucleosidase activity; IDA:TAIR.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008477; F:purine nucleosidase activity; IBA:GO_Central.
DR GO; GO:0045437; F:uridine nucleosidase activity; IDA:TAIR.
DR GO; GO:0072585; F:xanthosine nucleotidase activity; IDA:TAIR.
DR GO; GO:0006152; P:purine nucleoside catabolic process; IMP:TAIR.
DR GO; GO:0006218; P:uridine catabolic process; IMP:TAIR.
DR Gene3D; 3.90.245.10; -; 1.
DR InterPro; IPR001910; Inosine/uridine_hydrolase_dom.
DR InterPro; IPR023186; IUNH.
DR InterPro; IPR036452; Ribo_hydro-like.
DR PANTHER; PTHR12304; PTHR12304; 1.
DR Pfam; PF01156; IU_nuc_hydro; 1.
DR SUPFAM; SSF53590; SSF53590; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..336
FT /note="Uridine nucleosidase 1"
FT /id="PRO_0000394502"
FT ACT_SITE 29
FT /evidence="ECO:0000269|PubMed:30787180"
FT ACT_SITE 260
FT /evidence="ECO:0000250"
FT MUTAGEN 29
FT /note="D->A: Abrogated hydrolase activity."
FT /evidence="ECO:0000269|PubMed:30787180"
SQ SEQUENCE 336 AA; 36086 MW; B8BDEC584FB6C57E CRC64;
MDCGMENCNG GISNGDVLGK HEKLIIDTDP GIDDSMAILM AFQTPELEIL GLTTVFGNVS
TQDATRNALL LCEIAGFPDV PVAEGSSEPL KGGIPRVADF VHGKNGLGDV SLPPPSRKKS
EKSAAEFLDE KVEEYPGEVT ILALGPLTNL ALAIKRDSSF ASKVKKIVIL GGAFFSLGNV
NPAAEANIYG DPEAADVVFT SGADITVVGI NITTQLKLSD DDLLELGNCK GKHSKLISDM
CKFYRDWHVK SDGVYGVYLH DPVSFVAVVR PDLFTYKKGV VRVETQGICV GHTLMDQGLK
RWNGSNPWVG YSPISVAWTV DVEGVLEYVK AKLMKP
